Zobrazeno 1 - 10
of 19
pro vyhledávání: '"H S, Barra"'
Publikováno v:
Journal of Neuroscience Research. 28:171-181
We have used the monoclonal antibody YL 1/2 (Tyr) specific for tyrosinated tubulin, and a polyclonal antibody (Glu) specific for detyrosinated tubulin to visualize the distribution of microtubules and microtubule assembly sites during axonal outgrowt
Autor:
Carlos O. Arregui, H. S. Barra
Publikováno v:
Journal of Neuroscience Research. 27:256-263
We have used the monoclonal YL 1/2 (Tyr antibody) and polyclonal (Glu antibody) antibodies, specific for tyrosinated and detyrosinated tubulin, respectively, to determine the levels and cellular distribution of these tubulin species in chick retina d
Publikováno v:
Scopus-Elsevier
The beta-amyloid peptide (beta AP1-40) inhibited the in vitro post-translational incorporation of [14C]arginine at the N-terminus of brain soluble proteins and was labelled by the incorporation of [14C]arginine. Addition of arginine at the N-terminal
Publikováno v:
Molecular and cellular biochemistry. 216(1-2)
Membranes from brain tissue contain tubulin that can be isolated as a hydrophobic compound by partitioning into Triton X-114. The hydrophobic behavior of this tubulin is due to the formation of a complex with the alpha-subunit of Na+,K+-ATPase. In th
Publikováno v:
Journal of neuroscience research. 56(1)
We have previously reported the posttranslational addition of [14C]-arginine in the N-terminus of several soluble rat brain proteins. One of these proteins was identified as the microtubule-associated protein, the stable tubule only polypeptide (STOP
Publikováno v:
The Biochemical journal. 339
Tubulin carboxypeptidase is the enzyme that releases the C-terminal tyrosine from alpha-tubulin, converting tyrosine-terminated (Tyr) to detyrosinated (Glu) tubulin. The present study demonstrates that this enzyme is associated with microtubules in l
Publikováno v:
Molecular and cellular biochemistry. 170(1-2)
Brain membranes contain tubulin that can be isolated as a hydrophobic compound by partitioning into Triton X-114. We have previously postulated: (a) that this kind of tubulin is a peripheral membrane protein that arises from microtubules that in vivo
Publikováno v:
Molecular and cellular biochemistry. 170(1-2)
Tubulin carboxypeptidase, the enzyme which releases the COOH terminal tyrosine from the alpha-chain of tubulin, remains associated with microtubules through several cycles of assembly/disassembly (Arce CA, Barra HS: FEBS Lett 157: 75-78, 1983). Here,
Publikováno v:
Molecular and cellular biochemistry. 170(1-2)
A preparation of tubulin carboxypeptidase partially purified from bovine brain was found to contain a protein of molecular mass 30 kDa (P30) as determined by SDS-PAGE, that is recognized by a polyclonal anti-bovine pancreatic carboxypeptidase A. Howe
Publikováno v:
Neurochemical research. 22(4)
We demonstrate here that brain purified tubulin can be dissociated into alpha and beta subunits at pH10 and that the subunits can be separated by using the Triton X-114 phase separation system. After phase partition at pH10, alpha tubulin but not bet